메뉴 건너뛰기




Volumn 369, Issue 3, 2008, Pages 812-817

Crystal structure of Trypanosoma cruzi dihydroorotate dehydrogenase from Y strain

Author keywords

Cloning; Crystallization; Dihydroorotate dehydrogenase; Expression; Purification; Trypanosoma cruzi; X ray crystallography; Y strain

Indexed keywords

DIHYDROOROTATE DEHYDROGENASE; DIHYDROOROTIC ACID DERIVATIVE; FLAVINE MONONUCLEOTIDE; OROTIC ACID; PYRIMIDINE NUCLEOTIDE;

EID: 41149141262     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.02.074     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 0037135071 scopus 로고    scopus 로고
    • Parasitology-drugs to combat tropical protozoan parasites
    • Gelb M.H., and Hol W.G.J. Parasitology-drugs to combat tropical protozoan parasites. Science 297 (2002) 343-344
    • (2002) Science , vol.297 , pp. 343-344
    • Gelb, M.H.1    Hol, W.G.J.2
  • 2
    • 41149103647 scopus 로고    scopus 로고
    • World Health Organization, Control of Chagas Disease. Second report of the WHO Committee, WHO, Geneva, 2002, p.109.
    • World Health Organization, Control of Chagas Disease. Second report of the WHO Committee, WHO, Geneva, 2002, p.109.
  • 7
    • 0034945049 scopus 로고    scopus 로고
    • Specific molecular targets to control tropical diseases
    • Rodriguez J.B. Specific molecular targets to control tropical diseases. Current Pharmaceutical Design 7 (2001) 1105-1116
    • (2001) Current Pharmaceutical Design , vol.7 , pp. 1105-1116
    • Rodriguez, J.B.1
  • 8
    • 14644431768 scopus 로고    scopus 로고
    • The origin of dihydroorotate dehydrogenase genes of kinetoplastids, with special reference to their biological significance and adaptation to anaerobic, parasitic conditions
    • Annoura T., Nara T., Makiuchi T., Hashimoto T., and Aoki T. The origin of dihydroorotate dehydrogenase genes of kinetoplastids, with special reference to their biological significance and adaptation to anaerobic, parasitic conditions. Journal of Molecular Evolution 60 (2005) 113-127
    • (2005) Journal of Molecular Evolution , vol.60 , pp. 113-127
    • Annoura, T.1    Nara, T.2    Makiuchi, T.3    Hashimoto, T.4    Aoki, T.5
  • 10
    • 0018823799 scopus 로고
    • Pyrimidine nucleotide biosynthesis in animals - genes, enzymes, and regulation of UMP biosynthesis
    • Jones M.E. Pyrimidine nucleotide biosynthesis in animals - genes, enzymes, and regulation of UMP biosynthesis. Annual Review of Biochemistry 49 (1980) 253-279
    • (1980) Annual Review of Biochemistry , vol.49 , pp. 253-279
    • Jones, M.E.1
  • 11
    • 0041433824 scopus 로고    scopus 로고
    • E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases
    • Norager S., Jensen K.F., Bjornberg O., and Larsen S. E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure 10 (2002) 1211-1223
    • (2002) Structure , vol.10 , pp. 1211-1223
    • Norager, S.1    Jensen, K.F.2    Bjornberg, O.3    Larsen, S.4
  • 14
    • 41149141088 scopus 로고    scopus 로고
    • Defects in visicle core induced by Escherichia coli DHODH
    • Couto S.G., Nonato M.C., and Costa-Filho A.J. Defects in visicle core induced by Escherichia coli DHODH. Biophysical Journal 94 (2008) 1746-1753
    • (2008) Biophysical Journal , vol.94 , pp. 1746-1753
    • Couto, S.G.1    Nonato, M.C.2    Costa-Filho, A.J.3
  • 15
    • 33646860532 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of Leishmania major dihydroorotate dehydrogenase
    • Feliciano P.R., Cordeiro A.T., Costa A.J., and Nonato M.C. Cloning, expression, purification, and characterization of Leishmania major dihydroorotate dehydrogenase. Protein Expression and Purification 48 (2006) 98-103
    • (2006) Protein Expression and Purification , vol.48 , pp. 98-103
    • Feliciano, P.R.1    Cordeiro, A.T.2    Costa, A.J.3    Nonato, M.C.4
  • 17
    • 0031423109 scopus 로고    scopus 로고
    • Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis
    • Bjornberg O., Rowland P., Larsen S., and Jensen K.F. Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis. Biochemistry 36 (1997) 16197-16205
    • (1997) Biochemistry , vol.36 , pp. 16197-16205
    • Bjornberg, O.1    Rowland, P.2    Larsen, S.3    Jensen, K.F.4
  • 18
    • 0031568812 scopus 로고    scopus 로고
    • The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis
    • Rowland P., Nielsen F.S., Jensen K.F., and Larsen S. The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis. Structure 5 (1997) 239-252
    • (1997) Structure , vol.5 , pp. 239-252
    • Rowland, P.1    Nielsen, F.S.2    Jensen, K.F.3    Larsen, S.4
  • 19
    • 0029800334 scopus 로고    scopus 로고
    • The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers
    • Nielsen F.S., Andersen P.S., and Jensen K.F. The B form of dihydroorotate dehydrogenase from Lactococcus lactis consists of two different subunits, encoded by the pyrDb and pyrK genes, and contains FMN, FAD, and [FeS] redox centers. Journal of Biological Chemistry 271 (1996) 29359-29365
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 29359-29365
    • Nielsen, F.S.1    Andersen, P.S.2    Jensen, K.F.3
  • 21
    • 32944467057 scopus 로고    scopus 로고
    • Post-crystallization treatments for improving diffraction quality of protein crystals
    • Heras B., and Martin J.L. Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallographica Section D-Biological Crystallography 61 (2005) 1173-1180
    • (2005) Acta Crystallographica Section D-Biological Crystallography , vol.61 , pp. 1173-1180
    • Heras, B.1    Martin, J.L.2
  • 22
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. Journal of Applied Crystallography 26 (1993) 795-800
    • (1993) Journal of Applied Crystallography , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 23
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. Journal of Applied Crystallography 30 (1997) 1022-1025
    • (1997) Journal of Applied Crystallography , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 27
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D.I., and Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 29
    • 2642708353 scopus 로고    scopus 로고
    • The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function
    • Rowland P., Bjornberg O., Nielsen F.S., Jensen K.F., and Larsen S. The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function. Protein Science 7 (1998) 1269-1279
    • (1998) Protein Science , vol.7 , pp. 1269-1279
    • Rowland, P.1    Bjornberg, O.2    Nielsen, F.S.3    Jensen, K.F.4    Larsen, S.5
  • 30
    • 0036839243 scopus 로고    scopus 로고
    • The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers
    • Ottosen M.B., Bjornberg O., Norager S., Larsen S., Palfey B.A., and Jensen K.F. The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers. Protein Science 11 (2002) 2575-2583
    • (2002) Protein Science , vol.11 , pp. 2575-2583
    • Ottosen, M.B.1    Bjornberg, O.2    Norager, S.3    Larsen, S.4    Palfey, B.A.5    Jensen, K.F.6
  • 32
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical-clustering
    • Corpet F. Multiple sequence alignment with hierarchical-clustering. Nucleic Acids Research 16 (1988) 10881-10890
    • (1988) Nucleic Acids Research , vol.16 , pp. 10881-10890
    • Corpet, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.